Results 141 to 150 of about 6,174 (170)

Structural determinants of nucleobase modification recognition in the AlkB family of dioxygenases

open access: yesDNA Repair, 2020
Iron-dependent dioxygenases of the AlkB protein family found in most organisms throughout the tree of life play a major role in oxidative dealkylation processes. Many of these enzymes have attracted the attention of researchers across different fields and have been subjected to thorough biochemical characterization because of their link to human health
Johan Robben   +2 more
exaly   +4 more sources
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A Fix on AlkB

Science of Aging Knowledge Environment, 2002
After almost 2 decades of scrutiny, a mysterious DNA-repair protein has bared its inner workings. By mixing a set of ingredients never before known to be used by enzymes with that function, two research groups have deduced its mechanism. The studies reveal that the protein works differently from other DNA fix-it proteins and repairs defects in a single
openaire   +1 more source

Selective Inhibitors of AlkB Family of Nucleic Acid Demethylases

Biochemistry, 2019
The α-ketoglutarate-dependent (AlkB) superfamily of FeII/2-oxoglutarate (2-OG)-dependent dioxygenases consists of a unique class of nucleic acid repair enzymes that reversibly remove alkyl substituents from nucleobases through oxidative dealkylation.
Li-Jun Xie, Li Liu, Liang Cheng
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Molecular cloning and characterization of the alkB gene of Escherichia coli

Molecular and General Genetics MGG, 1985
Using methods of in vitro recombination we constructed hybrid plasmids that can suppress the increased methylmethane sulfonate sensitivity caused by alkB mutation. Since the cloned DNA fragment was mapped at 47 min on the Escherichia coli K12 genetic map, an area where the alkB gene is located, we concluded that the cloned DNA fragment contains the ...
H, Kataoka, M, Sekiguchi
openaire   +2 more sources

Genetic Diversity at alkB Locus in Brucella abortus

Journal of Veterinary Medicine, Series B, 2003
SummaryDNA polymorphism of the alkB gene, a DNA repair gene, was assessed by PCR on Brucella abortus biovars 1 (strains 99, S19, 45/20, RB51 and 2308), 3 (Tulya strain), 5 (B3196 strain) and 6 (870 strain). A DNA repetitive element, named IS711, was detected in all studied biovars 1 and its complete nucleotide sequence was determined. We found that the
C, Marianelli   +5 more
openaire   +2 more sources

AlkB and Its Homologues – DNA Repair and Beyond

2015
AlkB is an Fe(ii)/2-oxoglutarate-dependent dioxygenase that is part of the adaptive response to alkylating agents in Escherichia coli. AlkB hydroxylates a wide variety of alkylated DNA bases producing unstable intermediates which decompose to restore the non-alkylated bases. Homologues exist in other bacteria, metazoa (e.g.
Tina A. Müller, Robert P. Hausinger
openaire   +1 more source

A DFT Study of Nucleobase Dealkylation by the DNA Repair Enzyme AlkB

The Journal of Physical Chemistry B, 2009
Oxidative dealkylation is a unique mechanistic pathway found in the alpha-ketoglutarate-Fe(II)-dependent AlkB family of enzymes to remove the alkylation damage to DNA bases and regenerate nucleobases to their native state. The B3LYP density functional combined with a self-consistent reaction field was used to explore the triplet, quintet, and septet ...
Haining, Liu   +2 more
openaire   +2 more sources

Structural and mechanistic insight into alkane hydroxylation by Pseudomonas putida AlkB

Biochemical Journal, 2014
Pseudomonas putida GPo1 alkane hydroxylase (AlkB) is an integral membrane protein that catalyses the hydroxylation of medium-chain alkanes (C3–C12). 1-Octyne irreversibly inhibits this non-haem di-iron mono-oxygenase under turnover conditions, suggesting that it acts as a mechanism-based inactivator.
Alonso, Hernan   +7 more
openaire   +4 more sources

DFT study of a model system for the dealkylation step catalyzed by AlkB

Interdisciplinary Sciences: Computational Life Sciences, 2010
E. coli AlkB is a DNA repair enzyme that catalyzes the de-methylation of DNA by means of a non-heme iron and alpha-keto glutarate as a co-factor. The proposed reaction mechanism can be separated in four stages. The first stage involves the binding of the co-factor and molecular oxygen to the Fe in the active site. This is followed by the formation of a
openaire   +2 more sources

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